Production of monoclonal antibody (mAb) and purification thereof continue to pose a problem due to the high cost of the process. Contributing to the high cost are the several purification steps the biomolecules need to go through during isolation. For example, one of the purification steps is protein A affinity chromatography, wherein Staphylococcal protein A binds IgG molecules of subclasses 1, 2, and 4 with high selectivity and minimal interaction with the Fab region, the active region of the drug molecule. With the biotechnology market rapidly growing, improvements in these purification steps are becoming more desirable and more valuable in bringing biologics to the market in a timely space and at reduced cost.
During protein purification, polishing steps using anion exchanger media require that the media are not only selective to impurities but also tolerate feedstocks with high salt conductivities, for example, up to 15 mS/cm or more.
The foregoing shows that there exists an unmet need for anion exchanger media that are not only selective to impurities but also tolerate feedstocks with high salt conductivities.